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Osmolyte effect on the stability and folding of a hyperthermophilic protein.
Proteins. 2008 Apr; 71(1):110-8.P

Abstract

Proteins are known to be stabilized by naturally occurring osmolytes such as amino acids, sugars, and methylamines. Here, we examine the effect of trimethylamine-N-oxide (TMAO) on the conformational stability of ribonuclease HII from a hyperthermophile, Thermococcus kodakaraensis (Tk-RNase HII), which inherently possesses high conformational stability. Heat- and guanidine hydrochloride-induced unfolding experiments demonstrated that the conformational stability of Tk-RNase HII in the presence of 0.5M TMAO was higher than that in the absence of TMAO at all examined temperatures. TMAO affected the unfolding and refolding kinetics of Tk-RNase HII to a similar extent. These results indicate that proteins are universally stabilized by osmolytes, regardless of their robustness, and suggest a stabilization mechanism by osmolytes, caused by the unfavorable interaction of osmolytes with protein backbones in the denatured state. Our results also imply that the basic protein folding principle is not dependent on protein stability and evolution.

Authors+Show Affiliations

Department of Material and Life Science, Osaka University, Yamadaoka, Suita 565-0871, Japan.No affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

17932924

Citation

Mukaiyama, Atsushi, et al. "Osmolyte Effect On the Stability and Folding of a Hyperthermophilic Protein." Proteins, vol. 71, no. 1, 2008, pp. 110-8.
Mukaiyama A, Koga Y, Takano K, et al. Osmolyte effect on the stability and folding of a hyperthermophilic protein. Proteins. 2008;71(1):110-8.
Mukaiyama, A., Koga, Y., Takano, K., & Kanaya, S. (2008). Osmolyte effect on the stability and folding of a hyperthermophilic protein. Proteins, 71(1), 110-8.
Mukaiyama A, et al. Osmolyte Effect On the Stability and Folding of a Hyperthermophilic Protein. Proteins. 2008;71(1):110-8. PubMed PMID: 17932924.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Osmolyte effect on the stability and folding of a hyperthermophilic protein. AU - Mukaiyama,Atsushi, AU - Koga,Yuichi, AU - Takano,Kazufumi, AU - Kanaya,Shigenori, PY - 2007/10/13/pubmed PY - 2008/4/4/medline PY - 2007/10/13/entrez SP - 110 EP - 8 JF - Proteins JO - Proteins VL - 71 IS - 1 N2 - Proteins are known to be stabilized by naturally occurring osmolytes such as amino acids, sugars, and methylamines. Here, we examine the effect of trimethylamine-N-oxide (TMAO) on the conformational stability of ribonuclease HII from a hyperthermophile, Thermococcus kodakaraensis (Tk-RNase HII), which inherently possesses high conformational stability. Heat- and guanidine hydrochloride-induced unfolding experiments demonstrated that the conformational stability of Tk-RNase HII in the presence of 0.5M TMAO was higher than that in the absence of TMAO at all examined temperatures. TMAO affected the unfolding and refolding kinetics of Tk-RNase HII to a similar extent. These results indicate that proteins are universally stabilized by osmolytes, regardless of their robustness, and suggest a stabilization mechanism by osmolytes, caused by the unfavorable interaction of osmolytes with protein backbones in the denatured state. Our results also imply that the basic protein folding principle is not dependent on protein stability and evolution. SN - 1097-0134 UR - https://www.unboundmedicine.com/medline/citation/17932924/Osmolyte_effect_on_the_stability_and_folding_of_a_hyperthermophilic_protein_ L2 - https://doi.org/10.1002/prot.21660 DB - PRIME DP - Unbound Medicine ER -